• Journal of Power System Engineering
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• v.9 no.4
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• pp.148-154
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• 2005

Thermostable property is one of most important characteristics of graphite. Commercial graphites sheet from expanded graphite is using for high-temperature elements. Nowadays the new plant with high performance is developed in field of chemical industries, so the need of graphites is increasing rapidly. In this paper, the thermostable properties of newly developed graphite products with high density is investigated. I introduced the graphite material which developed for these heat tests by NGF method in order to test thermostable properties by comparing to the results of the commercial graphite sheet from expanded graphite in same condition. Through measuring the weight reducing ratio with various specimens in some conditions, I investigated the thermostable characteristics of these materials. It is verified that the graphite products by NGF method has almost same or superior thermostable properties comparing with that of commercial graphite sheet. Also the graphite products by NGF method have possibility of being better in thermostable properties.

• Korean Journal of Veterinary Research
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• v.21 no.2
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• pp.99-104
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• 1981

A total of 251 clinical isolates (human origin, 43 strains and bovine udder origin 208 strains) of the Staphylococcus that fermented mannitol aerobically were tested for their ability to produce coagulase, DNase, and thermostable nuclease. Of these, 158 isolates coagulated human or bovine plasma, produced DNase, and thermostable, nuclease and were identified as St. aureous, 146 of which produced a 1+ to 3+ clot. The remaining 12 isolated produced a -clot in citrate treated plasma but produced 1+ to 3+ clot in ethylenedi-aminetetraacetic acid (EDTA) treated plasma. It was found that 7 coagulase positive isolates failed to produced thermostable nuclease. In these organisms, we found out of the clot formation is not by coagulase activity but utilization of citrate, because EDTA treated plasma is not coagulated. Among 93 isolates which did not coagulate citrate-or EDTA treated plasma and thermostable nuclease negative, 28 strains produced DNase were identified as St. epidermidis, and other strains were not identification further. It was found that thermostable nuclese production appears to be a consistent property of St. aureus and the test is easy to perform, is rapid became quite distinct within 2 to 4 hour, and is not influenced by as many factors and variations as the coagulase test.

• Textile Coloration and Finishing
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• v.9 no.5
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• pp.82-87
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• 1997

Modified polypropylene was made of melt blending using thermostable-filler and polypropylene polymers. Modified PP were characterized for the purpose of improving a thermal-property of PP polymer with the composition of 5wt %, 10wt % of thermostable-filler. The structure and thermal-property were determined from IR, DSC, TGA, and SEM instruments. From the results of this study, it found the following facts. Firstly, it was found that the modified PP was mixed with PP and thermostable-filler qualitativly. Secondaty, thermal property of modified PP was improved steadily according to increase of ratio of thermostable-filler.

• Food Science and Biotechnology
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• v.18 no.3
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• pp.655-660
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• 2009

Biotechnological phytase preparations are commercially available and are currently used in animal feeding. However, thermostability constraints, low yields, and the high cost of the enzyme have limited its use. This study represents a new perspective for the food enzyme market. The research screened thermostable yeast strains for their ability to produce phytase. The screening was carried out with a gradual increase in temperature ($30-48^{\circ}C$). Sixteen strains (1 strain identified as Saccharomyces cerevisiae) maintained the ability to produce phytase at $48^{\circ}C$ and their phytase activity was confirmed using 2 phytase assay methodologies. The yeast strains tested in this study seem to be potential efficient producers of phytase, indicating a possible new source of thermostable phytase of commercial interest, particularly that from S. cerevisiae.

• Proceedings of the Korean Society of Precision Engineering Conference
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• 2012.05a
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• pp.995-996
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• 2012

• Proceedings of the Korean Society of Life Science Conference
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• 2006.09a
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• pp.91.2-91.2
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• 2006

• Proceedings of the Korean Society of Life Science Conference
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• 2007.10a
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• pp.54.2-54.2
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• 2007

See Full Text

• Proceedings of the Microbiological Society of Korea Conference
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• 1991.04a
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• pp.225-236
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• 1991

The genes encoding the thermostable $\alpha$-amylase and maltogenic amylase from Bacillus lichenciformis were cloned and expressed in E. coli. The recombinant plasmid pTA322 was found to contain a 3.1kb EcoRI genomic DNA fragment of the thermostable $\alpha$-amylase. The cloned $\alpha$-amylase was compared with the B. licheniformis native $\alpha$-amylase. Both $\alpha$-amylase have the same optimal temperature of $70^{\circ}C$ and are stable in the pH range of 6 and 9. The complete nucleotide sequences of the thermostable $\alpha$-amylase gene were determined. It was composed of one open reading rame of 1,536 bp. Start and stop codons are ATG and TAG. From the amino acid sequence deduced from the nucleotide sequence, the cloned thermostable $\alpha$-amylase is composed of 483 amino acid residues and its molecular weight is 55,200 daltons. The content of guanine and cytosine is $47.46mol\%$ and that of third base codon was $53_41mol\%$. The recombinant plasmid, pIJ322 encoding the maltogenic amylase contains a 3.5kb EcoRI-BamHI genomic DNA fragment. The optimal reaction temperature and pH of the maltogenci amylase were $50^{\circ}C$ and 7, respectively. The maltogenic amylase was capable of hydrolysing pullulan, starch and cyclodextrin to produce maltose from starch and panose from pullulan. The maltogenic amylase also showed the transferring activity. The maltogenic amylase gene is composed of one open reading frame of 1,734bp. Start and stop codons are ATG and ATG. At 2bp upstream from start codon, the nucleotide sequence AAAGGGGGAA seems to be the ribosome-binding site(RBS, Shine-Dalgarno sequence). A putative promoter(-35 and-10 regions) was found to be GTTAACA and TGATAAT. From deduced amino acid sequence from the nucleotide srquence, this enzyme was comosed of 578 amino acid residues and its molecular weight was 77,233 daltons. The content of guanine and cytosine was $48.1mol\%$. The new recombinant plasmid, pTMA322 constructed by inserting the thermostable $\alpha$-amylase gene in the EcoRI site of pIJ322 to produce both the thermostable $\alpha$-amylase and the maltogenic amylase were expressed in the E. coli. The two enzymes expressed from E. coli containing pTMA322 was reacted with the $15\%$ starch slurry at $40^{\circ}C$ for 24hours. The distribution of the branched oligosaccharides produced by the single-step process was of the ratio 50 : 50 between small oligosaccharide up DP3 and large oligosaccharide above DP3.

• Journal of Microbiology and Biotechnology
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• v.8 no.3
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• pp.270-276
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• 1998

Extracellular ${\alpha}$-glucosidase was purified to homogeneity from moderately thermophilic Bacillus sp. DG0303. The thermostable ${\alpha}$-glucosidase was purified by ammonium sulfate fractionation, ion-exchange chromatography, preparative polyacrylamide gel electrophoresis (PAGE), and electroelution. The molecular weight of the enzyme was estimated to be 60 kDa by SDS-PAGE. The optimum temperature for the action of the enzyme was at $60^{\circ}C$. It had a half-life of 35 min at $60^{\circ}C$. The enzyme was stable at the pH range of 4.5~7.0 and had an optimum pH at 5.0. The enzyme preparation did not require any metal ion for activity. The thermostable ${\alpha}$-glucosidase hydrolyzed the ${\alpha}$-1,6-linkages in isomaltose, isomaltotriose, and panose, and had little or no activity with maltooligosaccharides and other polysaccharides. The $K_m$ (mM) for p-nitrophenyl-${\alpha}$-D-glucopyranoside (pNPG), panose, isomaltose, and isomaltotriose were 4.6, 4.7, 40.8, and 3.7 and the $V_{max}$(${\mu}mol{\cdot}min^-1$$mg^-1$) for those substrates were 5629, 1669, 3410, and 1827, respectively. The N-terminal amino acid sequence of the enzyme was MERVWWKKAV. Based on its substrate specificity and catalytic properties, the enzyme has been assigned to be an oligo-1,6-glucosidase.

• KSBB Journal
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• v.25 no.6
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• pp.565-571
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• 2010

To develop thermostable ethanol fermentative yeast strain for lignocellulosic simultaneous saccharification and fermentation, high ethanol producing yeast, Saccharomyces cerevisiae CHY1012 and thermostable yeast, Kluyveromyces marxianus CHY1703 were fused by protoplast fusion. The thermostable fusant, CHY1612 was identified as a Kluyveromyces marxianus by phenotypic and physiological characteristics, as well as molecular analysis based on the D1/D2 domains of the large subunit (26S) rDNA gene and the internally transcribed spacer (ITS) 1 + 2 regions. For lignocellulosic ethanol production, AFEX pretreated barley straw at $150^{\circ}C$ for 90 min was used in a simultaneous saccharification and fermentation (SSF) process using thermotolerant CHY1612. The SSF from 16% pretreated barley straw at $43^{\circ}C$ gave a saccharification ratio of 90.5%, a final ethanol concentration of 38.5 g/L, and a theoretical yield of 91.2%. These results show that K. marxianus CHY1612 has potential for lignocellulosic ethanol production through simultaneous saccharification and fermentation with further development of process.